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Crystal structure of P. aeruginosa OXA10
Analyse Crystal structure of P. aeruginosa OXA10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WZ5
- Type
- protein
- Length
- 980 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase oxa-10
- EC
- 3.5.2.6
- UniProt
- P14489
- Ligands
- 3VU, SO4, CO2
- Pockets
- 12 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-lactamase oxa-10 (EC 3.5.2.6) | protein | 244 | 38% helix, 24% strand | P14489 |
| C, D | Beta-lactamase oxa-10 (EC 3.5.2.6) | protein | 246 | 38% helix, 23% strand | P14489 |
Ligands and binding sites
- 3VU · {(3R)-6-[(3-amino-1,2,4-thiadiazol-5-yl)oxy]-1-hydroxy-4,5-dimethyl-1,3-dihydro-2,1-benzoxaborol-3-yl}acetic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 13 copies · chains A, B, C, D
- CO2 · Carbon dioxide · ion · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.70 | 0.91 | 36 | empty |
| 2 | 122 | 0.69 | 0.90 | 29 | SO4 |
| 3 | 122 | 0.68 | 0.90 | 32 | SO4 |
| 4 | 541 | 0.65 | 0.76 | 78 | 3VU |
| 5 | 97 | 0.65 | 0.90 | 25 | empty |
Interfaces
3 interfaces between chains.
- B–D · 1421 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1410 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 629 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 covalent, 2 modified (disulfide, covalent ligand, carboxylation).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P14489
- Elsewhere: RCSB PDB 4WZ5 · PDBe 4WZ5 · UniProt P14489
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